ArticleProtein science : a publication of the Protein Society1999
Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Article
- Enhanced production of L-arginine by improving carbamoyl phosphate supply in metabolically engineered Corynebacterium crenatum.Applied microbiology and biotechnology · 2021Article
- High-throughput fitness screening and transcriptomics identify a role for a type IV secretion system in the pathogenesis of Crohn's disease-associated Escherichia coli.Nature communications · 2021Article
- Regulation of carbamoylphosphate synthesis in Escherichia coli: an amazing metabolite at the crossroad of arginine and pyrimidine biosynthesis.Amino acids · 2018Review
- Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.Biology · 2018Review
- Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.PLoS computational biology · 2011Article
- Structural and biochemical insights into the mechanism of fosfomycin phosphorylation by fosfomycin resistance kinase FomA.Biochemistry · 2011Article
- Mutation of archaeal isopentenyl phosphate kinase highlights mechanism and guides phosphorylation of additional isoprenoid monophosphates.ACS chemical biology · 2010Article
- X-ray structures of isopentenyl phosphate kinase.ACS chemical biology · 2010Article
- X-ray structure and characterization of carbamate kinase from the human parasite Giardia lamblia.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Characterization of thermophilic archaeal isopentenyl phosphate kinases.Biochemistry · 2010Article
- Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis.The Journal of biological chemistry · 2008Article
- The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.The Journal of biological chemistry · 2008Article
- The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction.Journal of bacteriology · 2007Article
- UMP kinase from Streptococcus pneumoniae: evidence for co-operative ATP binding and allosteric regulation.The Biochemical journal · 2004Article
- Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis.Journal of bacteriology · 2002Article
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymes carbamoyl phosphate synthetase (CPS) and carbamate kinase (CK) make carbamoyl phosphate in the same way: by ATP-phosphorylation of carbamate. The carbamate used by CK is made chemically, whereas CPS itself synthesizes its own carbamate in a process involving the phosphorylation of bicarbonate. Bicarbonate and carbamate are analogs and the phosphorylations are carried out by homologous 40 kDa regions of the 120 kDa CPS polypeptide. CK can also phosphorylate bicarbonate and is a homodimer of a 33 kDa subunit that was believed to resemble the 40 kDa regions of CPS. Such belief is disproven now by the CK structure reported here. The structure does not conform to the biotin carboxylase fold found in the 40 kDa regions of CPS, and presents a new type of fold possibly shared by homologous acylphosphate-making enzymes. A molecular 16-stranded open beta-sheet surrounded by alpha-helices is the hallmark of the CK dimer. Each subunit also contains two smaller sheets and a large crevice found at the location expected for the active center. Intersubunit interactions are very large and involve a central hydrophobic patch and more hydrophilic peripheral contacts. The crevice holds a sulfate that may occupy the site of an ATP phosphate, and is lined by conserved residues. Site-directed mutations tested at two of these residues inactivate the enzyme. These findings support active site location in the crevice. The orientation of the crevices in the dimer precludes their physical cooperation in the catalytic process. Such cooperation is not needed in the CK reaction but is a requirement of the mechanism of CPSs.
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